Difference between revisions of "Part:BBa K4814005"
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| + | <h1>RPA1 (human)</h1> | ||
| + | To further design a system that can detect DNA breaks in vivo, we proposed a FRET (Förster resonance energy transfer) system using the interaction between ATRIP and RPA1. | ||
| + | |||
| + | Due to the double-strand breaks (DSBs), replication protein A (RPA) will bind to the single-stranded DNA (ssDNA) and recruit ATRIP complex. The RPA70 (RPA1) N-terminus interacts with the ATRIP. (Bhat, K.P. and Cortez, D, 2018) | ||
| + | (Maréchal, A. and Zou, L., 2015) | ||
| + | |||
| + | Dueva, R., & Iliakis, G. (2020) stated that ATRIP is one of the prominent RPA-interacting partners, playing a crucial role in the repair mechanism of DNA repairing and DNA damage checkpoints (Zou, Y., Liu, Y., Wu, X., & Shell, S. M., 2006). Moreover, the N-terminus of RPA1 (RPA70) is shown to be binding to the ATRIP protein (Xu, X., et al, 2008). Considering the protein size, we did not use the entire RPA, instead, we chose RPA1, the interacting domain, to design the FRET system. | ||
| + | |||
| + | References: | ||
| + | |||
| + | Bhat, K.P., & Cortez, D. (2018). RPA and RAD51: fork reversal, fork protection, and genome stability. Nature Structural & Molecular Biology, 25(6), 446-453. https://doi.org/10.1038/s41594-018-0075-z | ||
| + | |||
| + | Maréchal, A., & Zou, L. (2015). RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response. Cell Research, 25(1), 9-23. https://doi.org/10.1038/cr.2014.147 | ||
| + | |||
| + | Dueva, R., & Iliakis, G. (2020). Replication protein A: a multifunctional protein with roles in DNA replication, repair and beyond. NAR cancer, 2(3), zcaa022. https://doi.org/10.1093/narcan/zcaa022 | ||
| + | |||
| + | Zou, Y., Liu, Y., Wu, X., & Shell, S. M. (2006). Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responses. Journal of cellular physiology, 208(2), 267–273. https://doi.org/10.1002/jcp.20622 | ||
| + | |||
| + | Xu, X., Vaithiyalingam, S., Glick, G. G., Mordes, D. A., Chazin, W. J., & Cortez, D. (2008). The basic cleft of RPA70N binds multiple checkpoint proteins, including RAD9, to regulate ATR signaling. Molecular and cellular biology, 28(24), 7345–7353. https://doi.org/10.1128/MCB.01079-08 | ||
Revision as of 13:02, 28 September 2023
RPA1 (human)
To further design a system that can detect DNA breaks in vivo, we proposed a FRET (Förster resonance energy transfer) system using the interaction between ATRIP and RPA1.
Due to the double-strand breaks (DSBs), replication protein A (RPA) will bind to the single-stranded DNA (ssDNA) and recruit ATRIP complex. The RPA70 (RPA1) N-terminus interacts with the ATRIP. (Bhat, K.P. and Cortez, D, 2018) (Maréchal, A. and Zou, L., 2015)
Dueva, R., & Iliakis, G. (2020) stated that ATRIP is one of the prominent RPA-interacting partners, playing a crucial role in the repair mechanism of DNA repairing and DNA damage checkpoints (Zou, Y., Liu, Y., Wu, X., & Shell, S. M., 2006). Moreover, the N-terminus of RPA1 (RPA70) is shown to be binding to the ATRIP protein (Xu, X., et al, 2008). Considering the protein size, we did not use the entire RPA, instead, we chose RPA1, the interacting domain, to design the FRET system.
References:
Bhat, K.P., & Cortez, D. (2018). RPA and RAD51: fork reversal, fork protection, and genome stability. Nature Structural & Molecular Biology, 25(6), 446-453. https://doi.org/10.1038/s41594-018-0075-z
Maréchal, A., & Zou, L. (2015). RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response. Cell Research, 25(1), 9-23. https://doi.org/10.1038/cr.2014.147
Dueva, R., & Iliakis, G. (2020). Replication protein A: a multifunctional protein with roles in DNA replication, repair and beyond. NAR cancer, 2(3), zcaa022. https://doi.org/10.1093/narcan/zcaa022
Zou, Y., Liu, Y., Wu, X., & Shell, S. M. (2006). Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responses. Journal of cellular physiology, 208(2), 267–273. https://doi.org/10.1002/jcp.20622
Xu, X., Vaithiyalingam, S., Glick, G. G., Mordes, D. A., Chazin, W. J., & Cortez, D. (2008). The basic cleft of RPA70N binds multiple checkpoint proteins, including RAD9, to regulate ATR signaling. Molecular and cellular biology, 28(24), 7345–7353. https://doi.org/10.1128/MCB.01079-08